Identification of isoenzymes using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
Article first published online: 2 FEB 2006
Copyright © 2006 John Wiley & Sons, Ltd.
Rapid Communications in Mass Spectrometry
Volume 20, Issue 5, pages 725–732, 15 March 2006
How to Cite
Hardouin, J., Hubert-Roux, M., Delmas, A. F. and Lange, C. (2006), Identification of isoenzymes using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom., 20: 725–732. doi: 10.1002/rcm.2355
- Issue published online: 2 FEB 2006
- Article first published online: 2 FEB 2006
- Manuscript Accepted: 17 DEC 2005
- Manuscript Revised: 16 DEC 2005
- Manuscript Received: 27 OCT 2005
- La Région Haute-Normandie
The identification of isoforms is one of the great challenges in proteomics due to the large number of identical amino acids preventing their separations by two-dimensional electrophoresis. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) has become a rapid and sensitive tool in proteomics, notably with the new instrumental improvements. In this study, we used several acquisition modes of MALDI-TOFMS to identify isoforms of porcine glutathiones S-transferase. The use of multiple proteases coupled to the different acquisition modes of MALDI-TOFMS (linear, reflectron, post-source decay (PSD) and in-source decay, positive and negative modes) allowed the identification of two sequences. Moreover, a third sequence is pointed out from a PSD study of a tryptic ion revealing the modification of the amino acid tyrosine 146 to phenylalanine. Copyright © 2006 John Wiley & Sons, Ltd.